HYCB_ECOLI
ID HYCB_ECOLI Reviewed; 203 AA.
AC P0AAK1; P16428; Q2MAA5; Q46883;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Formate hydrogenlyase subunit 2;
DE Short=FHL subunit 2;
DE AltName: Full=Hydrogenase-3 component B;
GN Name=hycB; Synonyms=hevB; OrderedLocusNames=b2724, JW2694;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2187144; DOI=10.1111/j.1365-2958.1990.tb00590.x;
RA Boehm R., Sauter M., Boeck A.;
RT "Nucleotide sequence and expression of an operon in Escherichia coli coding
RT for formate hydrogenlyase components.";
RL Mol. Microbiol. 4:231-243(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Probable electron transfer protein for hydrogenase 3.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: FHL comprises of a formate dehydrogenase, unidentified
CC electron carriers and a hydrogenase (isoenzyme 3). In this non-energy
CC conserving pathway, molecular hydrogen and carbodioxide are released
CC from formate.
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DR EMBL; X17506; CAA35547.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69234.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75766.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76801.1; -; Genomic_DNA.
DR PIR; H65052; H65052.
DR RefSeq; NP_417204.1; NC_000913.3.
DR RefSeq; WP_001079186.1; NZ_STEB01000027.1.
DR AlphaFoldDB; P0AAK1; -.
DR SMR; P0AAK1; -.
DR BioGRID; 4262103; 9.
DR ComplexPortal; CPX-317; Formate hydrogenlyase-H/Hydrogenase-3 complex.
DR IntAct; P0AAK1; 4.
DR MINT; P0AAK1; -.
DR STRING; 511145.b2724; -.
DR PaxDb; P0AAK1; -.
DR PRIDE; P0AAK1; -.
DR EnsemblBacteria; AAC75766; AAC75766; b2724.
DR EnsemblBacteria; BAE76801; BAE76801; BAE76801.
DR GeneID; 58389199; -.
DR GeneID; 948002; -.
DR KEGG; ecj:JW2694; -.
DR KEGG; eco:b2724; -.
DR PATRIC; fig|1411691.4.peg.4017; -.
DR EchoBASE; EB0470; -.
DR eggNOG; COG1142; Bacteria.
DR HOGENOM; CLU_043374_3_0_6; -.
DR InParanoid; P0AAK1; -.
DR OMA; RTCPTKA; -.
DR PhylomeDB; P0AAK1; -.
DR BioCyc; EcoCyc:HYCBSMALL-MON; -.
DR BioCyc; MetaCyc:HYCBSMALL-MON; -.
DR PRO; PR:P0AAK1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR GO; GO:0015944; P:formate oxidation; IDA:ComplexPortal.
DR GO; GO:0006007; P:glucose catabolic process; IDA:ComplexPortal.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF13247; Fer4_11; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..203
FT /note="Formate hydrogenlyase subunit 2"
FT /id="PRO_0000159263"
FT DOMAIN 2..32
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 42..72
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 73..102
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 137..169
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 156
FT /note="V -> A (in Ref. 1; CAA35547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 21873 MW; 828042E504B00DBD CRC64;
MNRFVIADST LCIGCHTCEA ACSETHRQHG LQSMPRLRVM LNEKESAPQL CHHCEDAPCA
VVCPVNAITR VDGAVQLNES LCVSCKLCGI ACPFGAIEFS GSRPLDIPAN ANTPKAPPAP
PAPARVSTLL DWVPGIRAIA VKCDLCSFDE QGPACVRMCP TKALHLVDNT DIARVSKRKR
ELTFNTDFGD LTLFQQAQSG EAK
